Results 161 to 170 of about 4,619 (182)
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Selective Activation of Human Caseinolytic Protease P (ClpP)
Angewandte Chemie International Edition, 2018AbstractCaseinolytic protease P (ClpP) is the proteolytic component of the ClpXP protein degradation complex. Eukaryotic ClpP was recently found to act within the mitochondria‐specific unfolded protein response (UPRmt). However, its detailed function and dedicated regulation remain largely unexplored.
Matthias Stahl +9 more
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Design and synthesis of tailored human caseinolytic protease P inhibitors
Chemical Communications, 2018To expedite functional studies of human ClpP we introduce tailored small molecule inhibitors. These compounds are active against the proteolytic ClpXP complex. Target identification elucidates anti-proliferative effects against cancer cells.
Thomas F. Gronauer +7 more
openaire +4 more sources
International Journal of Biological Macromolecules, 2017
Ecumicin is a well-known and potent inhibitor of Mycobacterium tuberculosis. Although the target of ecumicin is caseinolytic protease C1 (ClpC1), the exact mechanism by which ecumicin inhibits ClpC1 has not been identified. To analyze ecumicin's action on ClpC1, site-directed mutagenesis was performed on its binding site. The estimated binding residues
In-Pil, Jung +4 more
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Ecumicin is a well-known and potent inhibitor of Mycobacterium tuberculosis. Although the target of ecumicin is caseinolytic protease C1 (ClpC1), the exact mechanism by which ecumicin inhibits ClpC1 has not been identified. To analyze ecumicin's action on ClpC1, site-directed mutagenesis was performed on its binding site. The estimated binding residues
In-Pil, Jung +4 more
openaire +4 more sources
Journal of the American Chemical Society, 2015
Caseinolytic protease P (ClpP) represents a central bacterial degradation machinery that is involved in cell homeostasis and pathogenicity. The functional role of ClpP has been studied by genetic knockouts and through the use of beta-lactones, which remain the only specific inhibitors of ClpP discovered to date.
Mathias W. Hackl +11 more
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Caseinolytic protease P (ClpP) represents a central bacterial degradation machinery that is involved in cell homeostasis and pathogenicity. The functional role of ClpP has been studied by genetic knockouts and through the use of beta-lactones, which remain the only specific inhibitors of ClpP discovered to date.
Mathias W. Hackl +11 more
openaire +5 more sources
The Mechanism of Caseinolytic Protease (ClpP) Inhibition
Angewandte Chemie International Edition, 2013Malte Gersch +9 more
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Food Research International, 2022
The protein extract of Moringa oleifera flowers is reported to have milk-clotting activity (MCA), but information regarding its protease is unclear. In this study, two milk-clotting proteases (MoFP 12 and MoFP 13) with molecular weights of 42.304 kDa and 31.741 kDa, respectively, were isolated and identified from M.
Qiong, Zhao +5 more
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The protein extract of Moringa oleifera flowers is reported to have milk-clotting activity (MCA), but information regarding its protease is unclear. In this study, two milk-clotting proteases (MoFP 12 and MoFP 13) with molecular weights of 42.304 kDa and 31.741 kDa, respectively, were isolated and identified from M.
Qiong, Zhao +5 more
openaire +2 more sources
Journal of Natural Products, 2022
Staphylococcus aureus, especially drug-resistant S. aureus infections, is a worldwide healthcare challenge. There is a growing focus on antivirulence therapy against S. aureus. Caseinolytic protease p (ClpP) is a protein hydrolase essential for pathogenicity in S. aureus.
Wu Song +12 more
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Staphylococcus aureus, especially drug-resistant S. aureus infections, is a worldwide healthcare challenge. There is a growing focus on antivirulence therapy against S. aureus. Caseinolytic protease p (ClpP) is a protein hydrolase essential for pathogenicity in S. aureus.
Wu Song +12 more
openaire +2 more sources
Journal of Hepatology, 2002
Antibodies to caseinolytic protease P(177-194) (ClpP(177-194)) of the proteolytic subunit of the Clp complex of Escherichia coli (E. coli) are uniquely present in primary biliary cirrhosis (PBC). Molecular mimicry between the regulatory subunit ClpX and the principal T-cell epitope of pyruvate dehydrogenase complex (PDC-E2) in PBC, has been proposed to
Bogdanos, D P +6 more
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Antibodies to caseinolytic protease P(177-194) (ClpP(177-194)) of the proteolytic subunit of the Clp complex of Escherichia coli (E. coli) are uniquely present in primary biliary cirrhosis (PBC). Molecular mimicry between the regulatory subunit ClpX and the principal T-cell epitope of pyruvate dehydrogenase complex (PDC-E2) in PBC, has been proposed to
Bogdanos, D P +6 more
openaire +3 more sources
31–27 kDa Caseinolytic Protease in Human Tears
1998Normal wound healing requires the presence and regulation of cell adhesion proteins, proteases, and growth and other factors. Several of the proteases involved in tissue remodeling and wound healing have been detected in tear fluid. Previous studies on ocular pathologies have focused on the plasminogen-plasmin system1,2 and its role in fibrinolysis ...
M, Sakata +3 more
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